Carbon fixation in photosynthetic organisms
ASN 34;SER 36;ASP 66;THR 67(Potassium);GLU 222;ASP 246(Magnesium)
ASN 51;SER 53;ASP 84;THR 85(Potassium);GLU 242;ASP 266(Magnesium)
ASN 51;SER 53;ASP 83;THR 84(Potassium);GLU 240;ASP 264(Magnesium)
ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Magnesium)
ASN 674;SER 676;ASP 712;THR 713(Potassium);GLU 871;ASP 895(Magnesium)
ASN 1274;SER 1276;ASP 1312;THR 1313(Potassium);GLU 1471;ASP 1495(Magnesium)
ASN 1874;SER 1876;ASP 1912;THR 1913(Potassium);GLU 2071;ASP 2095(Magnesium)
ASN 3074;SER 3076;ASP 3112;THR 3113(Potassium);GLU 3271;ASP 3295(Magnesium)
ASN 3674;SER 3676;ASP 3712;THR 3713(Potassium);GLU 3871;ASP 3895(Magnesium)
ASN 4274;SER 4276;ASP 4312;THR 4313(Potassium);GLU 4471;ASP 4495(Magnesium)
ASN 4874;SER 4876;ASP 4912;THR 4913(Potassium);GLU 5071;ASP 5095(Magnesium)
ASN 74;SER 76;ASP 112;THR 113(Potassium);GLU 271;ASP 295(Manganese)
ASN 118;SER 120;ASP 156;THR 157(Potassium);GLU 315;ASP 339(Magnesium)
ASN 75;SER 77;ASP 113;THR 114(Potassium);GLU 272;ASP 296(Magnesium)
The allosteric regulation of pyruvate kinase.
Nuclear relaxation studies of the role of the divalent cation in the mechanism of pyruvate kinase and enolase: inner sphere and second sphere complexes.
Three-dimensional structure of cat muscle pyruvate kinase at 6 Angstrom resolution.
Three-dimensional structure of cat muscle pyruvate kinase at 3-1 A resolution.
Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution.
Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 A.
The structure and function of pyruvate kinase.
Muscle and liver pyruvate kinases are closely related: amino acid sequence comparisons.
Fluorine NMR studies on stereochemical aspects of reactions catalyzed by transcarboxylase, pyruvate kinase, and enzyme I.
7Li, 31P, and 1H NMR studies of interactions between ATP, monovalent cations, and divalent cation sites on rabbit muscle pyruvate kinase.
The structure of cat muscle pyruvate kinase.
Identification of tyrosine and lysine peptides labeled by 5'-p-fluorosulfonylbenzoyl adenosine in the active site of pyruvate kinase.
Crystallographic studies on the structure and catalytic activity of pyruvate kinase from skeletal muscle.
Structure of the oxalate-ATP complex with pyruvate kinase: ATP as a bridging ligand for the two divalent cations.
Nuclear Overhauser effect studies of the conformations of MgATP bound to the active and secondary sites of muscle pyruvate kinase.
Yeast pyruvate kinase: essential lysine residues in the active site.
Domain interaction in rabbit muscle pyruvate kinase. II. Small angle neutron scattering and computer simulation.
Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor.
2-[(4-Bromo-2,3-dioxobutyl)thio]-1,N6-ethenoadenosine 5'-diphosphate. A new fluorescent affinity label of a tyrosyl residue in the active site of rabbit muscle pyruvate kinase.
Cysteinyl peptides of rabbit muscle pyruvate kinase labeled by the affinity label 8-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5'-triphosphate.
Crystallization and preliminary analysis of enzyme-substrate complexes of pyruvate kinase from rabbit muscle.
The cooperative binding of fructose-1,6-bisphosphate to yeast pyruvate kinase.
Conformation of MgATP bound to nucleotidyl and phosphoryl transfer enzymes 1H-transferred NOE measurements on complexes of methionyl tRNA synthetase and pyruvate kinase.
Cysteinyl peptides labeled by dibromobutanedione in reaction with rabbit muscle pyruvate kinase.
Stereochemistry of metal ion coordination to the terminal thiophosphoryl group of adenosine 5'-O-(3-thiotriphosphate) at the active site of pyruvate kinase.
Two-dimensional transferred nuclear Overhauser effect spectroscopy study of the confirmation of MgATP bound at the active and ancillary sites of rabbit muscle pyruvate kinase.
Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate.
Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition.
Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A.
Effects of conserved residues on the regulation of rabbit muscle pyruvate kinase.
Ligand-induced conformational changes in wild-type and mutant yeast pyruvate kinase.
Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution.
The monovalent cation requirement of rabbit muscle pyruvate kinase is eliminated by substitution of lysine for glutamate 117.
Allostery in rabbit pyruvate kinase: development of a strategy to elucidate the mechanism.
Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel.
Conformational changes in yeast pyruvate kinase studied by 205Tl+ NMR.
Cooperativity in Bacillus stearothermophilus pyruvate kinase.
The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate.
Role of lysine 240 in the mechanism of yeast pyruvate kinase catalysis.
The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity.
Anion-induced folding of rabbit muscle pyruvate kinase: existence of multiple intermediate conformations at low pH.
Leishmania pyruvate kinase: the crystal structure reveals the structural basis of its unique regulatory properties.
Dimethylsulfoxide promotes K+-independent activity of pyruvate kinase and the acquisition of the active catalytic conformation.
Structural and functional linkages between subunit interfaces in mammalian pyruvate kinase.
Kinetic and allosteric consequences of mutations in the subunit and domain interfaces and the allosteric site of yeast pyruvate kinase.
Molecular and regulatory properties of leucoplast pyruvate kinase from Brassica napus (rapeseed) suspension cells.
Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.
Effects of metabolites on the structural dynamics of rabbit muscle pyruvate kinase.
Monitoring active site alterations upon mutation of yeast pyruvate kinase using 205Tl+ NMR.
Proton donor in yeast pyruvate kinase: chemical and kinetic properties of the active site Thr 298 to Cys mutant.
Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis.
This enzyme binds a potassium ion and two magnesium ions as cofactors. The first magnesium ion is bound to usbtrate, phosphoenolpyruvate, and acidic residues, whereas the second magnesium ion is bound to phosphate groups of the second substrate, ADP, without any interaction with protein residues. Thus, the second magnesium gets bound to the enzyme along with ADP binding. The potassium ion is bound to the transferred group, phosphate group of phosphoenolpyruvate. This enzyme catalyzes two reactions, firstly phoshoryl transfer and secondly isomerization, as follows (see [36], [39], [40] & [52]): (A) Transfer of phosphate group from phosphenolpyruvate to ADP: (A1) The negative charge of the acceptor group, the beta-phosphate of ADP, is stabilized by the second magnesium ion along with Arg119 (of 1a49;PDB). The negative charge of the transferred group is stabilized by the potassium ion and the two magnesium ion, along with Arg72, Lys269 and Arg119. The leaving oxygen atom of phosphoenolpyruvate is stabilized by the first magnesium ion and Lys269. (A2) The acceptor group, makes a nucleophilic attack on the transferred group, phosphate group of phosphoenolpyruvate, forming enolate intermediate. (This reaction seems associative (or SN2-like), according to the literature [39]). (B) Isomerization; Shift of double-bond (from C=C-O to C-C=O): (B1) The first magnesium ion binds the enolate oxygen atom of the intermediate, and stabilizes the negative charge on it. Lys269 also may stabilize it. (B2) A general acid must protonate the C3 atom (sp2 carbon atom) of the enolate intermediate, changing it to the methyl group (sp3 carbon). Initially, Lys269 was thought to be the general acid (see [10]). However, according to the more recent literature [36], a conserved acidic residue, Glu363, act as a general acid to protonate the sp2 carbon of the intermediate, through water molecules, Ser361 and Thr327. (The carbon atom interacts with a water molecule, which in turn interacts with Thr327. Thr327 interacts with Ser361 through a water, and Ser361 interacts with Glu363 through a water)